Results 121 to 130 of about 18,308,335 (162)

Protein S-sulfhydration: an emerging regulatory layer with therapeutic potential in metabolic dysfunction-associated steatotic liver disease. [PDF]

Hepatobiliary Surg Nutr
Pang M, Yang H.
europepmc   +1 more source

Mercaptopyruvate acts as endogenous vasodilator independently of 3-mercaptopyruvate sulfurtransferase activity

Nitric Oxide - Biology and Chemistry, 2018
Hydrogen sulfide (H2S) is produced by the action of cystathionine-β-synthase (CBS), cystathionine-γ-lyase (CSE) or 3-mercaptopyruvate sulfurtransferase (3-MST). 3-MST converts 3-mercaptopyruvate (MPT) to H2S and pyruvate. H2S is recognized as an endogenous gaseous mediator with multiple regulatory roles in mammalian cells and organisms.
Danila Gurgone, Valentina Citi, Vincenzo Brancaleone   +2 more
exaly   +10 more sources

3-mercaptopyruvate sulfurtransferase resides on the inner mitochondrial membrane

Nitric Oxide - Biology and Chemistry
3-mercaptopyruvate sulfurtransferase (MPST) is an enzyme implicated in the generation of the gasotransmitter hydrogen sulfide (H2S). Unlike, the other two H2S-synthesizing enzymes cystathionine gamma lyase (CSE) and cystathionine beta synthase (CBS), MPST is found in the mitochondria.
Vassilios Myrianthopoulos, Vassilis Gorgoulis, Andreas Papapetropoulos   +2 more
exaly   +4 more sources

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Specificity studies of 3-mercaptopyruvate sulfurtransferase†

Journal of Biochemical Toxicology, 1995
Abstract3‐Mercaptopyruvate sulfurtransferase (E.C. 2.8.1.2; MST) is an enzyme believed to function in the endogenous cyanide (CN) detoxification system because it is capable of transferring sulfur from 3‐mercaptopyruvate (3‐MP) to CN, forming the less toxic thiocyanate (SCN). To date, 3‐MP is the only known sulfur‐donor substrate for MST.
Steven I Baskin
exaly   +3 more sources

Discovery of an Inhibitor for Bacterial 3-Mercaptopyruvate Sulfurtransferase that Synergistically Controls Bacterial Survival [PDF]

Cell Chemical Biology, 2020
H2S-producing enzymes in bacteria have been shown to be closely engaged in the process of microbial survival and antibiotic resistance. However, no inhibitors have been discovered for these enzymes, e.g., 3-mercaptopyruvate sulfurtransferase (MST). In the present study, we identified several classes of inhibitors for Escherichia coli MST (eMST) through
Benfang Helen Ruan, Fang Wu, Jing Yu
exaly   +3 more sources

The effect of three α-keto acids on 3-mercaptopyruvate sulfurtransferase activity†

Journal of Biochemical Toxicology, 1996
3-Mercaptopyruvate sulfurtransferase catalyzes the transfer of sulfur from 3-mercaptopyruvate to several possible acceptor molecules, one of which is cyanide. Because the transsulfuration of cyanide is the primary in vivo mechanism of detoxification, 3-mercaptopyruvate sulfurtransferase may function in the enzymatic detoxification of cyanide in vivo ...
Steven I Baskin
exaly   +3 more sources

Role of 3-mercaptopyruvate sulfurtransferase in cancer

Cellular Signalling
The enzyme 3-mercaptopyruvate sulfurtransferase (3-MST) is widely distributed across different biological entities and is essential for the production of hydrogen sulfide (H₂S). This enzyme functions both in the cytosol and mitochondria, and 3-MST mediates the reaction of 3-mercaptopyruvate (3-MP) with dihydrolipoic acid and thioredoxin to generate ...
Dongdong Wu, Ti Chu, Yan-Wen Wang
exaly   +3 more sources

Redox Regulation of Mammalian 3-Mercaptopyruvate Sulfurtransferase

2015
A cystine-catabolizing enzyme, 3-mercaptopyruvate sulfurtransferase catalyzes the trans-sulfuration reaction of mercaptopyruvate or thiosulfate to thiol-containing compounds or cyanide. During the catalytic process, persulfide is formed at the catalytic site cysteine residue and a sulfur-acceptor substrate donates the outer sulfur of the persulfide to ...
Noriyuki, Nagahara, Masatoshi, Nagano, Takaaki, Ito, Hidenori, Suzuki   +3 more
openaire   +2 more sources

Steady-state kinetics of 3-mercaptopyruvate sulfurtransferase from bovine kidney

Archives of Biochemistry and Biophysics, 1978
Abstract Mammalian 3-mercaptopyruvate sulfurtransferase (EC 2.8.1.2), purified to apparent homogeneity by a new procedure, was studied by steady-state kinetic methods. The enzyme-catalyzed transfer of a sulfur atom from 3-mercaptopyruvate either to 2-mercaptoethanol or to a second molecule of 3-mercaptopyruvate was found to proceed by a sequential ...
R, Jarabak, J, Westley
openaire   +2 more sources